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1XDT

COMPLEX OF DIPHTHERIA TOXIN AND HEPARIN-BINDING EPIDERMAL GROWTH FACTOR

Summary for 1XDT
Entry DOI10.2210/pdb1xdt/pdb
DescriptorDIPHTHERIA TOXIN, HEPARIN-BINDING EPIDERMAL GROWTH FACTOR (3 entities in total)
Functional Keywordscomplex (toxin-growth factor), diphtheria toxin, receptor, heparin-binding epidermal growth factor, epidermal growth factor, complex (toxin-growth factor) complex, complex (toxin/growth factor)
Biological sourceCorynebacterium diphtheriae
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Cellular locationHeparin-binding EGF-like growth factor: Secreted, extracellular space. Proheparin-binding EGF-like growth factor: Cell membrane; Single-pass type I membrane protein: Q99075
Total number of polymer chains2
Total formula weight67338.87
Authors
Louie, G.V.,Yang, W.,Bowman, M.E.,Choe, S. (deposition date: 1997-11-18, release date: 1998-02-25, Last modification date: 2024-10-23)
Primary citationLouie, G.V.,Yang, W.,Bowman, M.E.,Choe, S.
Crystal structure of the complex of diphtheria toxin with an extracellular fragment of its receptor.
Mol.Cell, 1:67-78, 1997
Cited by
PubMed Abstract: We describe the crystal structure at 2.65 A resolution of diphtheria toxin (DT) complexed 1:1 with a fragment of its cell-surface receptor, the precursor of heparin-binding epidermal-growth-factor-like growth factor (HBEGF). HBEGF in the complex has the typical EGF-like fold and packs its principal beta hairpin against the face of a beta sheet in the receptor-binding domain of DT. The interface has a predominantly hydrophobic core, and polar interactions are formed at the periphery. The structure of the complex suggests that part of the membrane anchor of the receptor can interact with a hinge region of DT. The toxin molecule is thereby induced to form an open conformation conducive to membrane insertion. The structure provides a basis for altering the binding specificity of the toxin, and may also serve as a model for other EGF-receptor interactions.
PubMed: 9659904
DOI: 10.1016/S1097-2765(00)80008-8
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.65 Å)
Structure validation

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数据于2024-11-06公开中

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